From previous work (Z01HL00405-07LCB) and present efforts, organic solvents (methanol, 2-chloroethanol, and trifluoroethanol, which are known helix-formers) have been shown to have no effect on producing structure within the reduced lysozyme monomer, but only a continued randomization. This observation supports the previously stated hypothesis that SS bond formation is essential for a major transition to native structure. In a continuing investigation of factors that influence the structural state of reduced lysozyme, N-acetyl glucosamine (NAG) has been found to alter the CD spectra of fully reduced lysozyme and its carboxymethyl (CM) derivative. Computer curve fitting studies indicate an increased helical content of 1-3% of the chain length, with a decrease in beta structure of similar magnitude. The observed changes, together with preliminary equilibrium dialysis studies, suggest an interaction between NAG and a rudimentary binding site, not known to exist in the reduced protein. Interactions of NAG and other substrate analogues with reduced lysozyme are under continuing investigation.